Polyproteins in structural biology

Thibaut Crépin, Christopher Swale, Alexandre Monod, Frederic Garzoni, Maxime Chaillet, Imre Berger

Research output: Contribution to journalReview article (Academic Journal)peer-review

11 Citations (Scopus)


Polyproteins are chains of covalently conjoined smaller proteins that occur in nature as versatile means to organize the proteome of viruses including HIV. During maturation, viral polyproteins are typically cleaved into the constituent proteins with different biological functions by highly specific proteases, and structural analyses at defined stages of this maturation process can provide clues for antiviral intervention strategies. Recombinant polyproteins that use similar mechanisms are emerging as powerful tools for producing hitherto inaccessible protein targets such as the influenza polymerase, for high-resolution structure determination by X-ray crystallography. Conversely, covalent linking of individual protein subunits into single polypeptide chains are exploited to overcome sample preparation bottlenecks. Moreover, synthetic polyproteins provide a promising tool to dissect dynamic folding of polypeptide chains into three-dimensional architectures in single-molecule structure analysis by atomic force microscopy (AFM). The recent use of natural and synthetic polyproteins in structural biology and major achievements are highlighted in this contribution.

Original languageEnglish
Pages (from-to)139-46
Number of pages8
JournalCurrent Opinion in Structural Biology
Publication statusPublished - Jun 2015

Bibliographical note

Crown Copyright © 2015. Published by Elsevier Ltd. All rights reserved.

Structured keywords

  • Bristol BioDesign Institute


  • Amino Acid Sequence
  • Animals
  • Crystallography, X-Ray/methods
  • Humans
  • Microscopy, Atomic Force/methods
  • Models, Molecular
  • Molecular Sequence Data
  • Polyproteins/chemistry
  • Protein Conformation
  • Protein Folding
  • Recombinant Proteins/chemistry
  • Viral Proteins/chemistry
  • Viruses/chemistry

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